Lipidic phase membrane protein serial femtosecond crystallography

Autor: R. Bruce Doak, Karol Nass, Uwe Weierstall, Holger Fleckenstein, Ryan Coffee, Helmut Hirsemann, Benjamin Erk, Lars Gumprecht, Tomas Ekeberg, Jan Davidsson, Mark S. Hunter, Filipe R. N. C. Maia, Andreas Hartmann, Carl Caleman, Nils Kimmel, Christoph Bostedt, Weixiao Yuan Wahlgren, Joachim Ullrich, Ilme Schlichting, Erik Malmerberg, Michael J. Bogan, Dmitri Starodub, Heike Soltau, M. Marvin Seibert, Stephan Stern, John D. Bozek, John C. H. Spence, Stephan Kassemeyer, Lothar Strüder, Georg Weidenspointner, Andrew V. Martin, Thomas A. White, Günter Hauser, Saša Bajt, Gergely Katona, Raymond G. Sierra, Daniel P. DePonte, Jakob Andreasson, David Arnlund, Anton Barty, Petra Fromme, Janos Hajdu, Richard A. Kirian, Lukas Lomb, Christian Reich, Daniel Rolles, Nicola Coppola, Linda C. Johansson, Richard Neutze, Henry N. Chapman, Joachim Schulz, Cornelia B. Wunderer, Benedikt Rudek, Mengning Liang, Stefano Marchesini, Heinz Graafsma, Francesco Stellato, Nicusor Timneanu, Artem Rudenko, Miriam Barthelmess, Andrew Aquila, Peter Holl, Robert Hartmann, Xiaoyu Wang, Robert L. Shoeman, Sascha W. Epp, Christina Y. Hampton, Lutz Foucar
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Zdroj: Nature Methods
Nature methods 9, 263-265 (2012). doi:10.1038/nmeth.1867
Nature methods
DOI: 10.1038/nmeth.1867
Popis: X-ray free electron laser (X-FEL)-based serial femtosecond crystallography is an emerging method with potential to rapidly advance the challenging field of membrane protein structural biology. Here we recorded interpretable diffraction data from micrometer-sized lipidic sponge phase crystals of the Blastochloris viridis photosynthetic reaction center delivered into an X-FEL beam using a sponge phase micro-jet.
Databáze: OpenAIRE